RL16_LACLM
ID RL16_LACLM Reviewed; 137 AA.
AC A2RNP8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342};
GN Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; OrderedLocusNames=llmg_2376;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
CC -!- FUNCTION: Binds 23S rRNA and is also seen to make contacts with the A
CC and possibly P site tRNAs. {ECO:0000255|HAMAP-Rule:MF_01342}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01342}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000255|HAMAP-Rule:MF_01342}.
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DR EMBL; AM406671; CAL98939.1; -; Genomic_DNA.
DR RefSeq; WP_011677158.1; NZ_WJVF01000005.1.
DR PDB; 5MYJ; EM; 5.60 A; BP=1-137.
DR PDBsum; 5MYJ; -.
DR AlphaFoldDB; A2RNP8; -.
DR SMR; A2RNP8; -.
DR STRING; 416870.llmg_2376; -.
DR EnsemblBacteria; CAL98939; CAL98939; llmg_2376.
DR GeneID; 61110420; -.
DR KEGG; llm:llmg_2376; -.
DR eggNOG; COG0197; Bacteria.
DR HOGENOM; CLU_078858_2_1_9; -.
DR OMA; KGAVEYW; -.
DR PhylomeDB; A2RNP8; -.
DR BioCyc; LLAC416870:LLMG_RS11910-MON; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR HAMAP; MF_01342; Ribosomal_L16; 1.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR000114; Ribosomal_L16.
DR InterPro; IPR020798; Ribosomal_L16_CS.
DR PANTHER; PTHR12220; PTHR12220; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PRINTS; PR00060; RIBOSOMALL16.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR01164; rplP_bact; 1.
DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1.
DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; tRNA-binding.
FT CHAIN 1..137
FT /note="50S ribosomal protein L16"
FT /id="PRO_1000054642"
SQ SEQUENCE 137 AA; 15343 MW; 1BB1BFD67F6CD169 CRC64;
MLVPKRVKHR REFRGKMRGY AKGGDTVSFG EYGLQATTSH WITNRQIEAA RIAMTRYMKR
NGQVWIKIFP HKSYTAKAIG VRMGSGKGAP EGWVAPVKRG VVMFELGGVD EATAREALRL
ASHKLPVKTK FVKRGEA